Extracellular production of an intact and biologically active human growth hormone by the Bacillus brevis system

作者: T Kajino , Y Saito , O Asami , Y Yamada , M Hirai

DOI: 10.1038/SJ.JIM.2900445

关键词: ExtracellularProteasesPeptide sequenceSignal peptideBiochemistryBrevibacillus brevisBiological activityProtease inhibitor (biology)HeterologousBiology

摘要: The characteristic features of the Bacillus brevis system are very high productivity heterologous proteins and low extracellular protease activity. However, degradation some proteins, especially mammalian can be observed resulted in a lowering protein productivity. By using mutant expressing levels proteases addition EDTA to medium, intact human growth hormone (hGH) was successfully produced with B. system. Signal peptide modification higher basicity amino terminal region hydrophobicity middle brought about twelve-fold increase hGH production. yield further elevated 240 mg L-1 by optimization culture conditions. Thus, biologically active mature efficiently directly medium

参考文章(2)
H. Yamagata, K. Nakahama, Y. Suzuki, A. Kakinuma, N. Tsukagoshi, S. Udaka, Use of Bacillus brevis for efficient synthesis and secretion of human epidermal growth factor Proceedings of the National Academy of Sciences of the United States of America. ,vol. 86, pp. 3589- 3593 ,(1989) , 10.1073/PNAS.86.10.3589
Chung Nan Chang, Michael Key, Barry Bochner, Herbert Heyneker, Gregory Gray, High-level secretion of human growth hormone by Escherichia coli. Gene. ,vol. 55, pp. 189- 196 ,(1987) , 10.1016/0378-1119(87)90279-4